Amyloid precursor protein fragment and acetylcholinesterase increase with cell confluence and differentiation in a neuronal cell line

Francisca C. Bronfman, Hugo L. Fernandez, Nibaldo C. Inestrosa

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

19 Citas (Scopus)

Resumen

This study addresses the developmental regulation of amyloid precursor protein (APP) fragments comprising the amyloid-β peptide (Aβ) and the amyloid-p promoting factor acetyicholinesterase (ACHE) in a mouse neuronal cell line (Neuro-2a). Results indicated that a 35-kDa amyloidogenic fragment of APP and the major molecular forms of AChE (G~1 and G~4) in Neuro-2a cells significantly increase with increasing levels of cell confluence. The foregoing molecules undergo further increases when neuroblastoma cells differentiate in the presence of dibutyryl cAMP. In contrast, a 17-kDa fragment of APP and butyrylcholinesterase were not affected by cell confluence or differentiation. These findings are the first to indicate that a selective Aβ-containing fragment of APP is subject to develop mental regulation. Moreover, our data show that the 35-kDa fragment and AChE forms respond in parallel to the same developmental stimuli, i.e., cell confluence and differentiation. This points to the existence of a functional relationship between both molecules, a notion that is consistent with the potential role that has been ascribed to AChE in both APP processing and the formation of amyloid deposits in Alzheimer's brains.

Idioma originalInglés
Páginas (desde-hasta)93-99
Número de páginas7
PublicaciónExperimental Cell Research
Volumen229
N.º1
DOI
EstadoPublicada - 25 nov 1996
Publicado de forma externa

Áreas temáticas de ASJC Scopus

  • Biología celular

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